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Universidad y Salud

Print version ISSN 0124-7107On-line version ISSN 2389-7066


RODRIGUEZ-VELASQUEZ, Javier et al. Mathematical characterization of binding between PfNBP-1 protein and erythrocyite by applying probability and entropy. Univ. Salud [online]. 2014, vol.16, n.2, pp.188-197. ISSN 0124-7107.

Objective: Study the Plasmodium falciparum Normocyte Binding Protein-1 (PfNBP-1), based on a method of physical-mathematical characterization previously developed for high binding peptides of malaria merozoite to erythrocyte, it was a possible ligand associated to an alternative invasion pathway. Materials and methods: 21 non overlapped peptides with size of 20 amino acids, including two of high binding were taken; the frequency of occurrence of the 20 essential amino acids in each position was quantified and probability, summation of probability and entropy were calculated, in order to mathematically differentiate high and low binding peptides. Later the same values were calculated for theoretical analogs peptides, where the critical amino acids confirmed experimentally were changed by glycine. Results: The experimentally validated high binding peptides of PfNBP-1, showed values of probability summation of probability and entropy located within the binding macrostate peptides and their theoretical analogues presented results that differed increasingly of the binding macrostate as critical amino acids were replaced by glycine. For the PfNBP-1 sequences of non-binding, it was found that the calculated values are different from those associated with the macrostate of binding, verifying that in 100% of cases studied is possible to mathematically differentiate binding and non-binding peptides. Conclusions: The probability and entropy allow adequately characterize the high-binding peptides of PfNBP-1, and show the mathematical order underlying the process of protein binding of malaria to the erythrocyte.

Keywords : Erythrocyte; binding sites; peptides; probability.

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